Abstract
The effect of terminal GLY114* deletion on the binding affinity of the PA-IIL lectin toward L: -fucose was investigated. Both experimental (isothermal titration calorimetry) and computational (molecular dynamics simulations) methods have shown that the deletion mutation decreases the L-fucose affinity. It implies that the PA-IIL saccharide binding affinity is influenced by the dimerization of the lectin. A detailed analysis of computational data confirms the key role of electrostatic interactions in the PA-IIL/saccharide binding.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adhesins, Bacterial / chemistry*
-
Adhesins, Bacterial / genetics
-
Adhesins, Bacterial / metabolism
-
Binding, Competitive
-
Calorimetry / methods
-
Computer Simulation
-
Crystallization
-
Escherichia coli / genetics
-
Fucose / chemistry*
-
Fucose / metabolism
-
Kinetics
-
Lectins / chemistry*
-
Lectins / genetics
-
Lectins / metabolism
-
Models, Molecular
-
Mutation*
-
Protein Binding
-
Protein Multimerization
-
Protein Structure, Quaternary
-
Protein Structure, Tertiary
-
Pseudomonas aeruginosa / genetics
-
Pseudomonas aeruginosa / metabolism
-
Recombinant Proteins / chemistry
-
Recombinant Proteins / metabolism
-
Sequence Deletion
-
Thermodynamics
Substances
-
Adhesins, Bacterial
-
Lectins
-
Recombinant Proteins
-
adhesin, Pseudomonas
-
Fucose